ID A0A0M9YSH8_9ACTN Unreviewed; 666 AA.
AC A0A0M9YSH8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN ORFNames=ADK57_30640 {ECO:0000313|EMBL:KOU60339.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU60339.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOU60339.1}.
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DR EMBL; LGDG01000237; KOU60339.1; -; Genomic_DNA.
DR RefSeq; WP_053752859.1; NZ_LGDG01000237.1.
DR AlphaFoldDB; A0A0M9YSH8; -.
DR STRING; 1415546.ADK57_30640; -.
DR PATRIC; fig|1415546.3.peg.6629; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 17..388
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 400..610
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 618..650
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 666 AA; 73114 MW; 21F2CAB1C3BABC5C CRC64;
MPSAAPHDRL PLAFGGDYNP EQWPQEVWEE DVRLMREAGV TMVSLGIFAW SRIEPRPGEY
DFEWLDRIIG MLHEAGIDVD LATPTVVPPA WFYRAHPDAL PVTREGVRLA FGSRGAICHS
NPHYRAAAAN ITSRIGERYG RHPAVVLWHV HNEYGAPVLT CYCDTCAAAF RAWLQDRYGT
LGALNQAWGT AFWGQLYGDW EEIGVPRATP TVGNPAQQLD FQRFADGQAR ANFRAERDIL
HHLSPGVPVT TNFMVAPSQC QSIDYWEWGK EVDLVTNDHY LITDGRRTHV NLALAADLTR
SVAGGAPWLL LEHSPSGINW QAHNPAKEPG QMARNSLGHV ARGSEGAMFF QWRQSRSGAE
KFHSSMLPHG GTGTRVWREV TDLGRRVADL ADLRGSRTRA DVAMVWSWDS WWAQSLEWRP
SQDLDARERL DAFYEALYDR HLTVDFFAPA GLGDVDPSRY PLLVVPQLYA APASVAADLE
RYVSRGGTLL VSCFSGIVDE HDAVHPGACP GALRDVLGLT VEEFDPLLPG ERIAVRTSHG
DAWEADVWSE YVVPGDGCET VAVFAGGRTA GRPALTRRAL GDGAAWYLAT RLTGADLAAV
VDLALADAGV TPVDLPRDVE LVVREGGSGA FRFAVNHTDA EVKVVLADGS RAAVPAGAVE
VFREPR
//
